ID   TBPB_HAEIN              Reviewed;         625 AA.
AC   P44971;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Transferrin-binding protein B;
DE            Short=TbpB {ECO:0000305};
DE   AltName: Full=Transferrin-binding protein 2 {ECO:0000303|PubMed:7542800};
DE   Flags: Precursor;
GN   Name=tbpB; Synonyms=tbp2 {ECO:0000303|PubMed:7542800};
GN   OrderedLocusNames=HI_0995;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
CC   -!- FUNCTION: Haemophilus acquires iron by extracting it from serum
CC       transferrin (TF) in its human host. Acts as a transferrin receptor and
CC       is required for transferrin utilization.
CC       {ECO:0000250|UniProtKB:Q4QLR5}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane
CC       {ECO:0000250|UniProtKB:Q4QLR5, ECO:0000255|PROSITE-ProRule:PRU00303};
CC       Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}. Cell surface
CC       {ECO:0000250|UniProtKB:Q4QLR5}.
CC   -!- SIMILARITY: Belongs to the TbpB family. {ECO:0000305}.
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DR   EMBL; L42023; AAC22657.1; -; Genomic_DNA.
DR   PIR; D64107; D64107.
DR   RefSeq; NP_439158.1; NC_000907.1.
DR   RefSeq; WP_005693338.1; NC_000907.1.
DR   AlphaFoldDB; P44971; -.
DR   SMR; P44971; -.
DR   STRING; 71421.HI_0995; -.
DR   TCDB; 1.B.14.2.12; the outer membrane receptor (omr) family.
DR   EnsemblBacteria; AAC22657; AAC22657; HI_0995.
DR   KEGG; hin:HI_0995; -.
DR   PATRIC; fig|71421.8.peg.1038; -.
DR   eggNOG; ENOG502Z93R; Bacteria.
DR   HOGENOM; CLU_024250_0_0_6; -.
DR   OMA; GWFAYPG; -.
DR   BioCyc; HINF71421:G1GJ1-1037-MON; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR   Gene3D; 2.40.128.240; -; 1.
DR   InterPro; IPR011250; OMP/PagP_b-brl.
DR   InterPro; IPR001677; TbpB_B_D.
DR   InterPro; IPR035316; TbpB_C-lobe.
DR   InterPro; IPR038197; TbpB_C-lobe_sf.
DR   InterPro; IPR035313; TbpB_N-lobe.
DR   Pfam; PF17484; TbpB_A; 1.
DR   Pfam; PF01298; TbpB_B_D; 2.
DR   Pfam; PF17483; TbpB_C; 1.
DR   SUPFAM; SSF56925; SSF56925; 2.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cell outer membrane; Lipoprotein; Membrane; Palmitate; Receptor;
KW   Reference proteome; Signal; Virulence.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           18..625
FT                   /note="Transferrin-binding protein B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT                   /id="PRO_0000018191"
FT   REGION          25..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          99..125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          275..298
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          584..610
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..125
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        275..290
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        584..607
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           18
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           18
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   625 AA;  69031 MW;  52EFBC97B5ED4E9A CRC64;
     MKSVPLISGG LSLFLSACSG GGGSFDVDDV SNPSSSKPRY QDDTSNQRKK SNLEKLSIPS
     LGGGMKLVAQ NLRGREPSLL NEDGYIIFSS LSKIEDDFKK ENQSQEPTIG SIDEPSETNS
     PQNHHGQQYV YSGLYYIQSW RNFSNGKFYS GYYGYAYYFG KQTATTLPVN GEATYKGTWS
     FITATERGKN YSLFSNSSGQ GYSRRSAISE DIDLENDQNN GETGLISQFS ADFGTKKLKG
     ELFYTKRKTN NQNYEKKKLY DIDANIYSNR FRGKVKPTEK DSEEHPFTRE GTLEGGFYGP
     NGEELGGKFL AGDKKVFGVF SAKETEETKQ KTLPKETLID GKLTTFSTKK PDATTSTTAN
     AKTDATTNAE NFTTKDISSF GEADYLLIDN YPVPLLPETE NSGDFATSKH YEVRDKTYKV
     EACCKNLSYV KFGMYYEDNK KNNKNETEQY HQFLLGLRTA SSKIPTTGNV KYRGSWFGYI
     SDGETSYSTT GDKRQDKNAV AEFDVNFAEK TLKGSLKRAD SQNPVFSIEA NFKNGGNAFT
     GTATAKDLVI DGKNSQTKNT PINITTKVNG AFYGPNASEL GGYFTYNGKN PTDKNSPTAS
     SPSNSEKARA AVVFGAKKQV ETNNK